Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules

Autores
Baez, M.V.; Boccaccio, G.L.
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Fil:Baez, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Boccaccio, G.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
J. Biol. Chem. 2005;280(52):43131-43140
Materia
Degradation
Genes
Proteins
RNA
Deadenylation
Gene expression
RNA-binding proteins
Cytology
messenger RNA
protein mSmaug 1
protein Smaug
protein Staufen
protein TIA 1
protein TIAR
repressor protein
RNA binding protein
unclassified drug
animal cell
article
cell granule
central nervous system
chromosome 14
cytoplasm
Drosophila
fibroblast
gene expression
genome
human
human cell
molecular recognition
nonhuman
nucleotide sequence
priority journal
protein degradation
protein expression
protein family
reporter gene
RNA sequence
RNA translation
stress
synapse
synaptosome
translation regulation
translation repression
Amino Acid Motifs
Animals
Blotting, Western
Cell Line
Central Nervous System
Cercopithecus aethiops
Chromosomes, Human, Pair 14
COS Cells
Cricetinae
Cytoplasm
Cytoplasmic Granules
DNA, Complementary
Drosophila
Drosophila Proteins
Fibroblasts
Gene Library
Hela Cells
Humans
Luciferases
Mice
Microscopy, Confocal
Microscopy, Fluorescence
Models, Genetic
Molecular Sequence Data
Neurons
Plasmids
Polyribosomes
Protein Binding
Protein Biosynthesis
Repressor Proteins
Reverse Transcriptase Polymerase Chain Reaction
RNA
RNA, Messenger
RNA-Binding Proteins
Synapses
Tissue Distribution
Transfection
Animalia
Mammalia
Murinae
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00219258_v280_n52_p43131_Baez

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oai_identifier_str paperaa:paper_00219258_v280_n52_p43131_Baez
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granulesBaez, M.V.Boccaccio, G.L.DegradationGenesProteinsRNADeadenylationGene expressionRNA-binding proteinsCytologymessenger RNAprotein mSmaug 1protein Smaugprotein Staufenprotein TIA 1protein TIARrepressor proteinRNA binding proteinunclassified druganimal cellarticlecell granulecentral nervous systemchromosome 14cytoplasmDrosophilafibroblastgene expressiongenomehumanhuman cellmolecular recognitionnonhumannucleotide sequencepriority journalprotein degradationprotein expressionprotein familyreporter geneRNA sequenceRNA translationstresssynapsesynaptosometranslation regulationtranslation repressionAmino Acid MotifsAnimalsBlotting, WesternCell LineCentral Nervous SystemCercopithecus aethiopsChromosomes, Human, Pair 14COS CellsCricetinaeCytoplasmCytoplasmic GranulesDNA, ComplementaryDrosophilaDrosophila ProteinsFibroblastsGene LibraryHela CellsHumansLuciferasesMiceMicroscopy, ConfocalMicroscopy, FluorescenceModels, GeneticMolecular Sequence DataNeuronsPlasmidsPolyribosomesProtein BindingProtein BiosynthesisRepressor ProteinsReverse Transcriptase Polymerase Chain ReactionRNARNA, MessengerRNA-Binding ProteinsSynapsesTissue DistributionTransfectionAnimaliaMammaliaMurinaeCytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.Fil:Baez, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Boccaccio, G.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00219258_v280_n52_p43131_BaezJ. Biol. Chem. 2005;280(52):43131-43140reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-10-23T11:18:15Zpaperaa:paper_00219258_v280_n52_p43131_BaezInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-23 11:18:17.183Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
spellingShingle Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
Baez, M.V.
Degradation
Genes
Proteins
RNA
Deadenylation
Gene expression
RNA-binding proteins
Cytology
messenger RNA
protein mSmaug 1
protein Smaug
protein Staufen
protein TIA 1
protein TIAR
repressor protein
RNA binding protein
unclassified drug
animal cell
article
cell granule
central nervous system
chromosome 14
cytoplasm
Drosophila
fibroblast
gene expression
genome
human
human cell
molecular recognition
nonhuman
nucleotide sequence
priority journal
protein degradation
protein expression
protein family
reporter gene
RNA sequence
RNA translation
stress
synapse
synaptosome
translation regulation
translation repression
Amino Acid Motifs
Animals
Blotting, Western
Cell Line
Central Nervous System
Cercopithecus aethiops
Chromosomes, Human, Pair 14
COS Cells
Cricetinae
Cytoplasm
Cytoplasmic Granules
DNA, Complementary
Drosophila
Drosophila Proteins
Fibroblasts
Gene Library
Hela Cells
Humans
Luciferases
Mice
Microscopy, Confocal
Microscopy, Fluorescence
Models, Genetic
Molecular Sequence Data
Neurons
Plasmids
Polyribosomes
Protein Binding
Protein Biosynthesis
Repressor Proteins
Reverse Transcriptase Polymerase Chain Reaction
RNA
RNA, Messenger
RNA-Binding Proteins
Synapses
Tissue Distribution
Transfection
Animalia
Mammalia
Murinae
title_short Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_full Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_fullStr Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_full_unstemmed Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
title_sort Mammalian smaug is a translational repressor that forms cytoplasmic foci similar to stress granules
dc.creator.none.fl_str_mv Baez, M.V.
Boccaccio, G.L.
author Baez, M.V.
author_facet Baez, M.V.
Boccaccio, G.L.
author_role author
author2 Boccaccio, G.L.
author2_role author
dc.subject.none.fl_str_mv Degradation
Genes
Proteins
RNA
Deadenylation
Gene expression
RNA-binding proteins
Cytology
messenger RNA
protein mSmaug 1
protein Smaug
protein Staufen
protein TIA 1
protein TIAR
repressor protein
RNA binding protein
unclassified drug
animal cell
article
cell granule
central nervous system
chromosome 14
cytoplasm
Drosophila
fibroblast
gene expression
genome
human
human cell
molecular recognition
nonhuman
nucleotide sequence
priority journal
protein degradation
protein expression
protein family
reporter gene
RNA sequence
RNA translation
stress
synapse
synaptosome
translation regulation
translation repression
Amino Acid Motifs
Animals
Blotting, Western
Cell Line
Central Nervous System
Cercopithecus aethiops
Chromosomes, Human, Pair 14
COS Cells
Cricetinae
Cytoplasm
Cytoplasmic Granules
DNA, Complementary
Drosophila
Drosophila Proteins
Fibroblasts
Gene Library
Hela Cells
Humans
Luciferases
Mice
Microscopy, Confocal
Microscopy, Fluorescence
Models, Genetic
Molecular Sequence Data
Neurons
Plasmids
Polyribosomes
Protein Binding
Protein Biosynthesis
Repressor Proteins
Reverse Transcriptase Polymerase Chain Reaction
RNA
RNA, Messenger
RNA-Binding Proteins
Synapses
Tissue Distribution
Transfection
Animalia
Mammalia
Murinae
topic Degradation
Genes
Proteins
RNA
Deadenylation
Gene expression
RNA-binding proteins
Cytology
messenger RNA
protein mSmaug 1
protein Smaug
protein Staufen
protein TIA 1
protein TIAR
repressor protein
RNA binding protein
unclassified drug
animal cell
article
cell granule
central nervous system
chromosome 14
cytoplasm
Drosophila
fibroblast
gene expression
genome
human
human cell
molecular recognition
nonhuman
nucleotide sequence
priority journal
protein degradation
protein expression
protein family
reporter gene
RNA sequence
RNA translation
stress
synapse
synaptosome
translation regulation
translation repression
Amino Acid Motifs
Animals
Blotting, Western
Cell Line
Central Nervous System
Cercopithecus aethiops
Chromosomes, Human, Pair 14
COS Cells
Cricetinae
Cytoplasm
Cytoplasmic Granules
DNA, Complementary
Drosophila
Drosophila Proteins
Fibroblasts
Gene Library
Hela Cells
Humans
Luciferases
Mice
Microscopy, Confocal
Microscopy, Fluorescence
Models, Genetic
Molecular Sequence Data
Neurons
Plasmids
Polyribosomes
Protein Binding
Protein Biosynthesis
Repressor Proteins
Reverse Transcriptase Polymerase Chain Reaction
RNA
RNA, Messenger
RNA-Binding Proteins
Synapses
Tissue Distribution
Transfection
Animalia
Mammalia
Murinae
dc.description.none.fl_txt_mv Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Fil:Baez, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Boccaccio, G.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
publishDate 2005
dc.date.none.fl_str_mv 2005
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00219258_v280_n52_p43131_Baez
url http://hdl.handle.net/20.500.12110/paper_00219258_v280_n52_p43131_Baez
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv J. Biol. Chem. 2005;280(52):43131-43140
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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